α-synuclein abnormalities trigger focal tau pathology, spreading to various brain areas in Parkinson disease.
Animals
Autopsy
Behavior, Animal
Brain
/ pathology
Cell Survival
/ drug effects
Dopaminergic Neurons
/ drug effects
Female
Humans
Interferon-beta
/ genetics
MPTP Poisoning
/ pathology
Macaca mulatta
Male
Mice
Mice, Knockout
Parkinson Disease
/ pathology
Pregnancy
Rats
Rats, Wistar
Recombinant Proteins
Tauopathies
/ pathology
alpha-Synuclein
/ genetics
tau Proteins
/ biosynthesis
6-OHDA
MPTP
P-tau
P-α-synuclein
Parkinson disease
neurodegeneration
Journal
Journal of neurochemistry
ISSN: 1471-4159
Titre abrégé: J Neurochem
Pays: England
ID NLM: 2985190R
Informations de publication
Date de publication:
05 2021
05 2021
Historique:
revised:
28
07
2020
received:
21
03
2020
accepted:
30
11
2020
pubmed:
3
12
2020
medline:
22
6
2021
entrez:
2
12
2020
Statut:
ppublish
Résumé
Parkinson disease (PD) is the second most common neurodegenerative disorder, whose prevalence is 2~3% in the population over 65. α-Synuclein aggregation is the major pathological hallmark of PD. However, recent studies have demonstrated enhancing evidence of tau pathology in PD. Despite extensive considerations, thus far, the actual spreading mechanism of neurodegeneration has remained elusive in a PD brain. This study aimed to further investigate the development of α-synuclein and tau pathology. We employed various PD models, including cultured neurons treated with either 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) or with recombinant α-synuclein. Also, we studied dopaminergic neurons of cytokine Interferon-β knock-out. Moreover, we examined rats treated with 6-hydroxydopamine, Rhesus monkeys administrated with MPTP neurotoxin, and finally, human post-mortem brains. We found the α-synuclein phosphorylation triggers tau pathogenicity. Also, we observed more widespread phosphorylated tau than α-synuclein with prion-like nature in various brain areas. We optionally removed P-tau or P-α-synuclein from cytokine interferon-β knock out with respective monoclonal antibodies. We found that tau immunotherapy suppressed neurodegeneration more than α-synuclein elimination. Our findings indicate that the pathogenic tau could be one of the leading causes of comprehensive neurodegeneration triggered by PD. Thus, we can propose an efficient therapeutic target to fight the devastating disorder.
Substances chimiques
Mapt protein, mouse
0
Recombinant Proteins
0
alpha-Synuclein
0
tau Proteins
0
Interferon-beta
77238-31-4
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
727-751Informations de copyright
© 2020 International Society for Neurochemistry.
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